Glucosamine-6-phosphate synthase (GlmS)

Glucosamine-6-phosphate synthase (GlmS) is a key enzyme catalyzing the conversion of fructose-6-phosphate and glutamine into glucosamine-6-phosphate, the first committed step in the biosynthesis of UDP-N-acetylglucosamine (UDP-GlcNAc)[5]. This reaction is vital for the formation of amino sugar-containing macromolecules, such as bacterial and fungal cell walls. Structurally, the enzyme contains two main active sites located on separate domains and mediates hydrolysis, intramolecular ammonia transfer, and isomerization steps[1]. Its essential function in cell wall biosynthesis makes it a validated antimicrobial target, with inhibitors explored for antibacterial, antifungal, and potential antidiabetic applications. In cancer and diabetes, altered GlmS activity has metabolic implications, including insulin resistance and aberrant glycosylation[5].

Other names

L-glutamine:D-fructose-6-phosphate amidotransferaseGlcN-6-P synthaseG6PSGlucosamine-6-P synthase

Inhibition of enzyme activity through occupation of active sites; prevents biosynthesis of essential amino sugars, thereby impeding cell wall production in bacteria and fungi[1][5]